1mzk: Difference between revisions

Revision as of 19:22, 27 July 2008

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File:1mzk.png

Template:STRUCTURE 1mzk

NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in ArabidopsisNMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis

Template:ABSTRACT PUBMED 14500786

About this StructureAbout this Structure

1MZK is a Single protein structure of sequence from Arabidopsis thaliana. Full experimental information is available from OCA.

ReferenceReference

NMR structure of the forkhead-associated domain from the Arabidopsis receptor kinase-associated protein phosphatase., Lee GI, Ding Z, Walker JC, Van Doren SR, Proc Natl Acad Sci U S A. 2003 Sep 30;100(20):11261-6. Epub 2003 Sep 18. PMID:14500786

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-'''NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis'''
+===NMR structure of kinase-interacting FHA domain of kinase associated protein phosphatase, KAPP in Arabidopsis===
-==Overview==
+<!--
-Forkhead-associated (FHA) domains are phosphoprotein-binding modules found in diverse signaling proteins that bind partners phosphorylated on threonine or serine. Kinase-associated protein phosphatase from Arabidopsis employs its FHA domain for negative regulation of receptor-like kinase signaling pathways, which are important in plant development. The solution structure of the free state of kinase-interacting FHA domain (KI-FHA) of kinase-associated protein phosphatase has been determined with high precision and accuracy using residual dipolar couplings. KI-FHA is a sandwich of a five-stranded mixed beta-sheet with a six-stranded antiparallel beta-sheet. Despite homology only in the recognition loops, this fold is shared with FHA domains from checkpoint proteins from yeast and humans, as well as with nonhomologous MH2 domains of Smad tumor suppressors. A shared pattern of hydrophobicity throughout FHA domains and Smad MH2 domains may stabilize the core of the beta-sandwich. Evolutionary trace analysis of FHA domains suggests class-specific residues in the recognition loops that could tune their phosphoprotein-binding specificity. This surface agrees with that of KI-FHA in contact with a phosphothreonine peptide ligand. Evolutionary trace analysis also predicts an unexpected swath of class-specific residues on another face of FHA domains. Protein interactions with these faces may affect assembly of transmembrane signaling complexes in plants, and in other FHA domain-containing assemblies.
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+{{ABSTRACT_PUBMED_14500786}}
 ==About this Structure==
-MZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA].
+MZK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MZK OCA].
 ==Reference==
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 [[Category: Walker, J C.]]
 [[Category: Beta sandwich]]
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